4WD3

Crystal structure of an L-amino acid ligase RizA

Summary for 4WD3

Entry DOI	10.2210/pdb4wd3/pdb
Related	3VMM 3VOT
Descriptor	L-amino acid ligase (1 entity in total)
Functional Keywords	l-amino acid ligase, atp-grasp domain, rhizocticin antibiotic biosynthesis, ligase
Biological source	Bacillus subtilis subsp. subtilis
Total number of polymer chains	2
Total formula weight	93905.48
Authors	Kagawa, W.,Arai, T.,Kino, K.,Kurumizaka, H. (deposition date: 2014-09-06, release date: 2015-09-09, Last modification date: 2024-10-16)
Primary citation	Kagawa, W.,Arai, T.,Ishikura, S.,Kino, K.,Kurumizaka, H. Structure of RizA, an L-amino-acid ligase from Bacillus subtilis. Acta Crystallogr.,Sect.F, 71:1125-1130, 2015 Cited by PubMed Abstract: RizA is an L-amino-acid ligase from Bacillus subtilis that participates in the biosynthesis of rhizocticin, an oligopeptide antibiotic. The substrate-free form of RizA has been crystallized and the structure was solved at 2.8 Å resolution. The amino-acid-binding site appears to be capable of accommodating multiple amino acids, consistent with previous biochemical studies. PubMed: 26323296 DOI: 10.1107/S2053230X15012698 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.8 Å)

Structure validation